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Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair.

This gene encodes a member of a subfamily of RING-finger type E3 ubiquitin ligases. The protein binds to specific DNA sequences, and recruits a histone deacetylase to regulate gene expression. Its expression peaks at late G1 phase and continues during G2 and M phases of the cell cycle. It plays a major role in the G1/S transition by regulating topoisomerase IIalpha and retinoblastoma gene expression, and functions in the p53-dependent DNA damage checkpoint. It is regarded as a hub protein for the integration of epigenetic information. This gene is up-regulated in various cancers, and it is therefore considered to be a therapeutic target. Multiple transcript variants encoding different isoforms have been found for this gene. A related pseudogene exists on chromosome 12. [provided by RefSeq, Feb 2014]

Gene RIF (98)

Results showed that UHRF1 was overexpressed in almost all of the prostate cancer cell (PCa) lines. Its expression levels were correlated with some clinical features of PCa suggesting it as an independent prognostic factor for biochemical recurrence.

describe a mechanism of interstrand crosslink (ICL) sensing and propose that UHRF1 is a critical factor that binds to ICLs. In turn, this binding is necessary for the subsequent recruitment of FANCD2, which allows the DNA repair process to initiate

Findings demonstrated the inhibitory effect of MEG3 in vivo and vitro and illuminated that MEG3 could be a potential biomarker for the survival of hepatocellular carcinoma (HCC) patients. Its expression seemed to be regulated by UHRF1 in HCC.

UHRF1 interacts with TopoIIalpha and regulates its localization to hemimethylated DNA. TopoIIalpha decatenates the hemimethylated DNA following replication, which might facilitate the methylation of the nascent strand by DNMT1

Results implicate UHRF1 as an oncogene and suggest that global DNA hypomethylation induced by UHRF1 overexpression induces a p53-mediated senescence program that is bypassed in hepatocellular carcinoma.

linked tandem Tudor & PHD of UHRF1 operates as a functional unit in cells, providing a defined combinatorial readout of a heterochromatin signature within a single histone H3 tail, essential for UHRF1-directed epigenetic inheritance of DNA methylation

UHRF1 contains linked two-histone reader modules tethered by a 17-aa linker, which plays a role as a functional switch involved in multiple regulatory pathways such as maintenance of DNA methylation and transcriptional repression.

results reveal that the disruption of Dnmt1/PCNA/UHRF1 interactions acts as an oncogenic event and that one of its signatures (i.e. the low level of mMTase activity) is a molecular biomarker associated with a poor prognosis in GBM patients

Knockdown of UHRF1 activates MDR1 promoter activity and expression, attenuates the binding of UHRF1 and HDAC1 to the MDR1 promoter.Overexpression of UHRF1 in NCI/ADR-RES cells can induce deacetylation of histones H3 and H4 on the MDR1 promoter

the 1.7 A crystal structure of the apo SRA domain of human UHRF1 and a 2.2 A structure of its complex with hemi-methylated DNA, revealing a previously unknown reading mechanism for methylated CpG sites (mCpG)